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What You Need to Know About Enzyme Therapy

Since the 1960s, scientists have been researching and developing enzyme drugs for medical treatment. These treatments can improve metabolism, fight infections, and promote tissue regeneration. Enzymes are the body’s means of fighting disease, enhancing wound healing, and promoting tissue regeneration. Still, the body must introduce enzymes at the right place and dosage to be effective. Read on to learn more about enzyme drugs and their use. Listed below are some of the most common enzyme drugs.


One of the most common adverse effects of asparaginase enzyme therapy is hypersensitivity to the enzyme. This reaction may occur in two forms: clinical and subclinical. Clinical hypersensitivity is a common cause of dose-limiting toxicity and is characterized by increased production of anti-asparaginase antibodies. Patients who develop this reaction may have lowered asparagine activity and have poorer outcomes than those who do not exhibit hypersensitivity. The use of asparaginase preparations derived from Erwinia chrysanthemi and pegylated asparaginase is recommended in patients who develop clinical hypersensitivity.

While PEG-asparaginase is less immunogenic than the native preparation, a small number of patients develop an allergic reaction to it. In these cases, PEG-asparaginase is recommended for patients whose immune response to asparaginase is not well-controlled by induction therapy. However, some studies have found an increased incidence of asparaginase hypersensitivity in PEG-asparaginase-treated patients.

There are other potential uses of PEG-asparaginase. It has been used in the treatment of acute myeloid leukemia (AML) and ovarian cancer. Other applications include the treatment of non-Hodkin lymphoma and sarcomas. Further studies are needed to identify whether PEG-asparaginase is an effective treatment for these cancers.

Patients who develop allergic reactions to asparaginase are usually switched to an alternative asparaginase formulation. Erwinia chrysanthemi is safe for patients who are sensitive to PEG-asparaginase. Its cross-reactivity with the E. coli-derived asparaginase is low, making it easier for patients to complete the treatment.

The activity of asparaginase is dependent on the autoprocessing of the substrate. Asparaginase activity increases as the autoprocessing process proceeds. In the case of ASRGL1, incomplete autocleavage results in low enzymatic activity. Genetic engineering has made it possible to achieve several modifications that increase autoprocessing efficiency in vitro. Although efforts have been made to produce alternative enzymes of bacterial origin, no such attempts have been successful.


Asparaginase is an enzyme that helps break down asparagine, an amino acid that some tumor cells need. It can inhibit the growth of tumor cells by blocking the formation of protein. It has been listed on the World Health Organization’s list of essential medicines. Patients take L-asparaginase by injection into a vein or muscle. Its benefits include anti-cancer activity, tumor remission, and reduced cancer cell viability.

Asparaginase is produced naturally by the bacterium Escherichia sp., although some research has also examined the role of this enzyme in treating the disease. It is beneficial in treating ALL, and research into the enzyme’s effect on acrylamide formation in foods has accelerated in recent years. Commercial L-asnase is produced by the bacterium Erwinia sp.

Asparaginase is commonly given by intramuscular injection and rarely as a subcutaneous injection. Asparaginase is passed into the buttock and upper thigh and causes a dull ache and stinging. Pegaspargase is usually injected through a cannula into a vein in the arm. However, asparaginase can have serious side effects if sensitive to the substance.

The anti-cancer properties of asparaginase were first recognized in 1953 when lymphomas in rats and mice were treated with guinea pig serum. This study revealed that asparaginase is a critical component of this protein, and it has become the definitive source for cancer treatment. Further, this enzyme is produced in large quantities in such a bacterium. Asparaginase is an effective treatment for various cancers, and researchers have been studying its use in human trials since 1978.

However, the most common side effects of enzyme treatment are the development of antibodies against L-asparaginase II produced by E. coli. Immune cells rapidly recognize these antibodies and neutralize the enzyme’s effect. Some patients may also experience an adverse reaction to the enzyme, even with a 50% reduction in the dose. This type of allergy may be particularly problematic if the patient has a genetic predisposition to the enzyme.